CNR ExploRA

Articolo in rivista, 2009, ENG, 10.1016/j.biocel.2008.09.009

Increased spermine oxidase (SMO) activity as a novel differentiation marker of myogenic C2C12 cells

Cervelli M.a; Fratini E.a,b; Amendola R.b; Bianchi M.a; Signori E.c; Ferraro E.d; Lisi A.c; Federico R.a; Marcocci L.e;, Mariottini P.a

a = Dipartimento di Biologia, Università Roma Tre, Rome, Italy; b = Dipartimento BAS-BiotecMed, ENEA, CR Casaccia, Rome, Italy; c = Istituto di Neurobiologia e Medicina Molecolare, CNR, Rome, Italy; d = Laboratory of Molecular Neuro-embryology, IRCCS Fondazione Santa Lucia, 00143 Rome, Italy; e = Dipartimento di Scienze Biochimiche A. Rossi Fanelli, Università La Sapienza, Rome, Italy.

Spermine oxidase (SMO) is a FAD-containing enzyme involved in animal cell polyamines (PA) homeostasis, selectively active on spermine and producing H(2)O(2), spermidine, and the 3-aminopropanal. In the present study, we have examined the SMO gene expression during the mouse myoblast C2C12 cell differentiation induced with two different stimuli by RT-PCR analysis, polysome-mRNP distribution and enzyme activity. SMO transcript accumulation and enzymatic activity increases during C2C12 cell differentiation and correlates with the decrease of spermine content. Many proteins are highly regulated during the phenotypic conversion of rapidly dividing C2C12 myoblasts into fully differentiated post-mitotic myotubes. The SMO gene induction represents a novel and additional marker of C2C12 cell differentiation. The sub-cellular localization of the SMOalpha and SMOmu splice variants is not involved in the differentiation processes. Nuclear localization of only the SMOmu protein was confirmed.

International journal of biochemistry & cell biology 41 (4), pp. 934–944